EC number:1.14.99.51

Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.99 Miscellaneous
ID:1.14.99.51
Description:Hercynylcysteine S-oxide synthase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.99.51
BRENDA Enzyme Link: BRENDA 1.14.99.51
KEGG Enzyme Link: KEGG1.14.99.51
BioCyc Enzyme Link: BioCyc 1.14.99.51
ExPASy Enzyme Link: ExPASy1.14.99.51
EC2PDB Enzyme Link: EC2PDB 1.14.99.51
ExplorEnz Enzyme Link: ExplorEnz 1.14.99.51
PRIAM enzyme-specific profiles Link: PRIAM 1.14.99.51
IntEnz Enzyme Link: IntEnz 1.14.99.51
MEDLINE Enzyme Link: MEDLINE 1.14.99.51

EC number:1.14.99.51

MSA:

1.14.99.51;
Phylogenetic Tree:

1.14.99.51;
Uniprot:
M-CSA:
RHEA:42704 hercynine + L-cysteine + O2 = H2O + S-(hercyn-2-yl)-L-cysteine S-oxide
RULE(radius=1) [*:1]-[SH;+0:2].[*:3]:[cH;+0:4]:[*:5].[O;H0;+0:6]=[O;H0;+0:7]>>[*:1]-[S;H0;+0:2](=[O;H0;+0:6])-[c;H0;+0:4](:[*:3]):[*:5].[OH2;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Participation of an intermediate sulfoxide in the enzymatic thiolation of the imidazole ring of hercynine to form ergothioneine.Ishikawa Y, Israel SE, Melville DB1974 Jul 254276459
Bioinformatic and biochemical characterizations of C-S bond formation and cleavage enzymes in the fungus Neurospora crassa ergothioneine biosynthetic pathway.Hu W, Song H, Sae Her A, Bak DW, Naowarojna N, Elliott SJ, Qin L, Chen X, Liu P2014 Oct 1725275953
Genetic and metabolomic dissection of the ergothioneine and selenoneine biosynthetic pathway in the fission yeast, S. pombe, and construction of an overproduction system.Pluskal T, Ueno M, Yanagida M201424828577